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Database: UniProt
Entry: A0A1E7FRH1_9STRA
LinkDB: A0A1E7FRH1_9STRA
Original site: A0A1E7FRH1_9STRA 
ID   A0A1E7FRH1_9STRA        Unreviewed;       707 AA.
AC   A0A1E7FRH1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-SEP-2023, entry version 21.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=FRACYDRAFT_259678 {ECO:0000313|EMBL:OEU20761.1};
OS   Fragilariopsis cylindrus CCMP1102.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae;
OC   Fragilariopsis.
OX   NCBI_TaxID=635003 {ECO:0000313|EMBL:OEU20761.1, ECO:0000313|Proteomes:UP000095751};
RN   [1] {ECO:0000313|EMBL:OEU20761.1, ECO:0000313|Proteomes:UP000095751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1102 {ECO:0000313|EMBL:OEU20761.1,
RC   ECO:0000313|Proteomes:UP000095751};
RG   DOE Joint Genome Institute;
RA   Mock T., Otillar R.P., Strauss J., Dupont C., Frickenhaus S., Maumus F.,
RA   Mcmullan M., Sanges R., Schmutz J., Toseland A., Valas R., Veluchamy A.,
RA   Ward B.J., Allen A., Barry K., Falciatore A., Ferrante M., Fortunato A.E.,
RA   Gloeckner G., Gruber A., Hipkin R., Janech M., Kroth P., Leese F.,
RA   Lindquist E., Lyon B.R., Martin J., Mayer C., Parker M., Quesneville H.,
RA   Raymond J., Uhlig C., Valentin K.U., Worden A.Z., Armbrust E.V., Bowler C.,
RA   Green B., Moulton V., Van Oosterhout C., Grigoriev I.;
RT   "Extensive genetic diversity and differential bi-allelic expression allows
RT   diatom success in the polar Southern Ocean.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC         aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC         Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC         ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001027};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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DR   EMBL; KV784354; OEU20761.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E7FRH1; -.
DR   EnsemblProtists; OEU20761; OEU20761; FRACYDRAFT_259678.
DR   KEGG; fcy:FRACYDRAFT_259678; -.
DR   InParanoid; A0A1E7FRH1; -.
DR   OrthoDB; 5399939at2759; -.
DR   Proteomes; UP000095751; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR005478; Transketolase_bac-like.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   NCBIfam; TIGR00232; tktlase_bact; 1.
DR   PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR   PANTHER; PTHR43522:SF10; TRANSKETOLASE; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095751};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..707
FT                   /note="transketolase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009193511"
FT   DOMAIN          55..75
FT                   /note="Transketolase signature 1"
FT                   /evidence="ECO:0000259|PROSITE:PS00801"
FT   REGION          136..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   707 AA;  76119 MW;  71386CE876371192 CRC64;
     MKFSSFAIAA VAIAASSVSA FSAPKFAVHQ PTFLMATAVD ADTKTALATA ANEARGLAMD
     SIAAAHSGHM GLPLGCAEIG ATLYGSQMSY NAADPQWLNR DRFILSAGHG SMFLYSWLNI
     AGFDLPMEEV KNFRQHHSRT PGHPEFPSSH HNTPGIESTT GPLGQGVSNA VGMAASEKMA
     AAVYNTDDHK IFDHHIFALA GDGCFQEGVS AESAAFAAHE KLDNLIILYD ANEVTLDKMA
     EYTQSEDIIK RYDAYGWETY DIDGHDLDAV EEAIAAAKAN NNGKPKFIKC NTIIGKGMEE
     TEGTNAAHGE AGVPYVEKAK KNIGIPEGEK WFVSEGTRDF FGDVQKKNIA TYDAWQTTFA
     SWEAANPDLA KQLKNAVEDN VMSAADMIKD IDAMGDDAEA TRVSGNKVIQ DISRLVPHYV
     SGSADLHGST RNYINEGGNF GSGFDKTYAG KNLYFGIREH AMGSIMNGFG FHGLFKVSGS
     TFLVFVDYFR PTVRVAALSE LGAVSYILTH DSIGVGEDGP THQPVETVSG LRVIPNLDVY
     RPADAEETVA AMVHSVTRKD GPTALIFSRQ NIDQNGEVDY MTRREGALKG AYIAKKETED
     LSLIVIATGS EVPHALKAAA TLPGARVVSM PCMEVYERQS AEYKESVLPS SCTKRIAMEA
     GVSDPWYKYA SKVVGVDKFG FSAPGDIVMT EYGMTPENLA AEIASMD
//
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